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P42321

- CATA_PROMI

UniProt

P42321 - CATA_PROMI

Protein

Catalase

Gene

katA

Organism
Proteus mirabilis
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

    Catalytic activityi

    2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

    Cofactori

    Heme group.
    NADP.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei54 – 541
    Active sitei127 – 1271
    Metal bindingi337 – 3371Iron (heme axial ligand)1 Publication

    GO - Molecular functioni

    1. catalase activity Source: UniProtKB-EC
    2. heme binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. hydrogen peroxide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    SABIO-RKP42321.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase (EC:1.11.1.6)
    Gene namesi
    Name:katA
    OrganismiProteus mirabilis
    Taxonomic identifieri584 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 484484CatalasePRO_0000084992Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531Methionine sulfone1 Publication

    Keywords - PTMi

    Oxidation

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    484
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 193
    Beta strandi22 – 243
    Helixi34 – 4310
    Beta strandi52 – 543
    Beta strandi56 – 6611
    Turni71 – 733
    Helixi77 – 793
    Beta strandi85 – 939
    Beta strandi95 – 973
    Beta strandi103 – 1075
    Beta strandi110 – 1178
    Beta strandi120 – 13011
    Helixi137 – 1393
    Helixi140 – 1478
    Turni151 – 1533
    Helixi158 – 1669
    Helixi169 – 1713
    Helixi172 – 1798
    Helixi181 – 1833
    Beta strandi184 – 1863
    Helixi188 – 1903
    Beta strandi199 – 2024
    Beta strandi208 – 21710
    Helixi226 – 23510
    Helixi239 – 24911
    Beta strandi255 – 26410
    Helixi265 – 2695
    Beta strandi271 – 2733
    Turni284 – 2863
    Beta strandi290 – 29910
    Helixi304 – 3074
    Turni308 – 3103
    Helixi328 – 34518
    Helixi349 – 3513
    Turni353 – 3553
    Beta strandi358 – 3603
    Beta strandi382 – 3843
    Beta strandi386 – 3883
    Helixi394 – 3963
    Helixi412 – 4143
    Helixi420 – 4289
    Helixi431 – 44515
    Helixi450 – 46314
    Helixi465 – 47814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E93X-ray2.00A1-484[»]
    1H6NX-ray2.11A1-484[»]
    1H7KX-ray2.40A2-484[»]
    1M85X-ray2.00A1-484[»]
    1MQFX-ray2.50A1-484[»]
    1NM0X-ray2.30A1-484[»]
    2CAGX-ray2.70A1-484[»]
    2CAHX-ray2.70A1-484[»]
    3HB6X-ray2.30A1-484[»]
    ProteinModelPortaliP42321.
    SMRiP42321. Positions 4-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42321.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the catalase family.Curated

    Family and domain databases

    Gene3Di2.40.180.10. 1 hit.
    InterProiIPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR024708. Catalase_AS.
    IPR024711. Catalase_clade1/3.
    IPR011614. Catalase_core.
    IPR002226. Catalase_haem_BS.
    IPR010582. Catalase_immune_responsive.
    [Graphical view]
    PANTHERiPTHR11465. PTHR11465. 1 hit.
    PfamiPF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
    PRINTSiPR00067. CATALASE.
    SMARTiSM01060. Catalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56634. SSF56634. 1 hit.
    PROSITEiPS00437. CATALASE_1. 1 hit.
    PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P42321-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKKKLTTAA GAPVVDNNNV ITAGPRGPML LQDVWFLEKL AHFDREVIPE    50
    RRMHAKGSGA FGTFTVTHDI TKYTRAKIFS EVGKKTEMFA RFSTVAGERG 100
    AADAERDIRG FALKFYTEEG NWDMVGNNTP VFYLRDPLKF PDLNHIVKRD 150
    PRTNMRNMAY KWDFFSHLPE SLHQLTIDMS DRGLPLSYRF VHGFGSHTYS 200
    FINKDNERFW VKFHFRCQQG IKNLMDDEAE ALVGKDRESS QRDLFEAIER 250
    GDYPRWKLQI QIMPEKEAST VPYNPFDLTK VWPHADYPLM DVGYFELNRN 300
    PDNYFSDVEQ AAFSPANIVP GISFSPDKML QGRLFSYGDA HRYRLGVNHH 350
    QIPVNAPKCP FHNYHRDGAM RVDGNSGNGI TYEPNSGGVF QEQPDFKEPP 400
    LSIEGAADHW NHREDEDYFS QPRALYELLS DDEHQRMFAR IAGELSQASK 450
    ETQQRQIDLF TKVHPEYGAG VEKAIKVLEG KDAK 484
    Length:484
    Mass (Da):55,614
    Last modified:November 1, 1995 - v1
    Checksum:iADC25F3CB41F5C50
    GO

    Mass spectrometryi

    Molecular mass is 55643±5 Da from positions 1 - 484. Determined by ESI. 1 Publication

    Sequence databases

    PIRiA58663.

    Cross-referencesi

    Sequence databases

    PIRi A58663.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E93 X-ray 2.00 A 1-484 [» ]
    1H6N X-ray 2.11 A 1-484 [» ]
    1H7K X-ray 2.40 A 2-484 [» ]
    1M85 X-ray 2.00 A 1-484 [» ]
    1MQF X-ray 2.50 A 1-484 [» ]
    1NM0 X-ray 2.30 A 1-484 [» ]
    2CAG X-ray 2.70 A 1-484 [» ]
    2CAH X-ray 2.70 A 1-484 [» ]
    3HB6 X-ray 2.30 A 1-484 [» ]
    ProteinModelPortali P42321.
    SMRi P42321. Positions 4-479.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P42321.

    Miscellaneous databases

    EvolutionaryTracei P42321.

    Family and domain databases

    Gene3Di 2.40.180.10. 1 hit.
    InterProi IPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR024708. Catalase_AS.
    IPR024711. Catalase_clade1/3.
    IPR011614. Catalase_core.
    IPR002226. Catalase_haem_BS.
    IPR010582. Catalase_immune_responsive.
    [Graphical view ]
    PANTHERi PTHR11465. PTHR11465. 1 hit.
    Pfami PF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
    PRINTSi PR00067. CATALASE.
    SMARTi SM01060. Catalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56634. SSF56634. 1 hit.
    PROSITEi PS00437. CATALASE_1. 1 hit.
    PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site."
      Buzy A., Bracchi V., Sterjiades R., Chroboczek J., Thibault P., Gagnon J., Jouve H.-M., Hudry-Clergeon G.
      J. Protein Chem. 14:59-72(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305, OXIDATION AT MET-53, MASS SPECTROMETRY.
      Strain: PR.
    2. "Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH."
      Gouet P., Jouve H.-M., Dideberg O.
      J. Mol. Biol. 249:933-954(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
      Strain: PR.
    3. "Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy."
      Gouet P., Jouve H.-M., Williams P.A., Andersson I., Andreoletti P., Nussaume L., Hajdu J.
      Nat. Struct. Biol. 3:951-956(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), ABSORPTION SPECTROSCOPY.
    4. "High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron."
      Andreoletti P., Sainz G., Jaquinod M., Gagnon J., Jouve H.-M.
      Proteins 50:261-271(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), EPR SPECTROSCOPY.

    Entry informationi

    Entry nameiCATA_PROMI
    AccessioniPrimary (citable) accession number: P42321
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3